1989
DOI: 10.1021/bi00450a021
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Hypelcin A, an .alpha.-aminoisobutyric acid containing antibiotic peptide, induced permeability change of phosphatidylcholine bilayers

Abstract: Interactions of hypelcin A, an alpha-aminoisobutyric acid containing antibiotic peptide, with phosphatidylcholine vesicles were investigated to obtain information on its bioactive mechanism. The peptide induced the leakage of a fluorescent dye, calcein, entrapped in sonicated vesicles. The leakage rate depended on both the peptide and the lipid concentrations. Analysis of this dependency indicated that the leakage was due to the monomeric peptide and that the membrane-perturbing activity of the monomer was hig… Show more

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Cited by 49 publications
(27 citation statements)
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“…In addition, although the phase transition of DPPG was altered by a high concentration of puroA, the enthalpy of the main transition is comparable to the enthalpy for pure DPPG, thus suggesting that puroA does not penetrate deeply into the hydrophobic region of DPPG vesicles. Based on these data, puroA most likely resides at the solvent-lipid interface because peptides or proteins interacting with the hydrophobic regions of membranes often exhibit large reductions in transition enthalpy (33). This, along with the observation that puroA decreased the temperature and cooperativity of the main phase transition of DPPG, is characteristic of an interfacial location in the phospholipid bilayer (35).…”
Section: Discussionmentioning
confidence: 86%
“…In addition, although the phase transition of DPPG was altered by a high concentration of puroA, the enthalpy of the main transition is comparable to the enthalpy for pure DPPG, thus suggesting that puroA does not penetrate deeply into the hydrophobic region of DPPG vesicles. Based on these data, puroA most likely resides at the solvent-lipid interface because peptides or proteins interacting with the hydrophobic regions of membranes often exhibit large reductions in transition enthalpy (33). This, along with the observation that puroA decreased the temperature and cooperativity of the main phase transition of DPPG, is characteristic of an interfacial location in the phospholipid bilayer (35).…”
Section: Discussionmentioning
confidence: 86%
“…Calcein leakage from vesicles has previously been used to indicate whether peptides were capable of forming pores in vesicle systems (27). Similar to other calcein‐leakage studies, the time course of the fluorescent marker release in EPG/EPC LUVs was followed by fluorescence spectroscopy.…”
Section: Resultsmentioning
confidence: 97%
“…Hydrophobic and charged residues are shown in dark and lighter tones respectively. Illustrations were generated with molmol.hydrophobic region of the peptide under neutral pH conditions.Calcein leakage assaysCalcein leakage from vesicles has previously been used to indicate whether peptides were capable of forming pores in vesicle systems(27). Similar to other calcein-leakage studies, the time course of the fluorescent marker release in EPG/EPC LUVs was followed by fluorescence spectroscopy.After addition of the peptide, the fluorescence was measured for up to 10 min.…”
mentioning
confidence: 99%
“…The result, at least in model membranes, is a significant disordering of lipid side chains and altered temperatures in the transition from the gel phase to the liquid-crystal phase. This effect alone might be sufficient to destabilize membranes and increase their permeability (11,22). It is also conceivable that, like ionomycin, mefloquine forms complexes with cations via its four-position hydroxyl group and piperidine functional groups and that it acts as a mobile ion carrier (Fig.…”
Section: Discussionmentioning
confidence: 99%